RNE_NEOYE
ID RNE_NEOYE Reviewed; 509 AA.
AC Q1XDS6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Ribonuclease E/G-like protein;
DE Short=RNase E/G-like protein;
DE EC=3.1.26.-;
GN Name=rne;
OS Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX NCBI_TaxID=2788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U-51;
RA Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in intercistronic processing of primary transcripts
CC from chloroplast operons. The endonucleolytic activity of the enzyme
CC depends on the number of phosphates at the 5' end, is inhibited by
CC structured RNA, and preferentially cleaves A/U-rich sequences.
CC {ECO:0000250|UniProtKB:F4IV66}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P21513};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P21513};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000250|UniProtKB:F4IV66}.
CC -!- SIMILARITY: Belongs to the RNase E/G family. {ECO:0000305}.
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DR EMBL; AP006715; BAE92335.1; -; Genomic_DNA.
DR RefSeq; YP_536892.1; NC_007932.1.
DR AlphaFoldDB; Q1XDS6; -.
DR SMR; Q1XDS6; -.
DR GeneID; 3978795; -.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR InterPro; IPR004659; RNase_E/G.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR30001; PTHR30001; 1.
DR Pfam; PF10150; RNase_E_G; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00757; RNaseEG; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Chloroplast; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW mRNA processing; Nuclease; Plastid; RNA-binding.
FT CHAIN 1..509
FT /note="Ribonuclease E/G-like protein"
FT /id="PRO_0000277283"
FT DOMAIN 35..117
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P21513"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P21513"
SQ SEQUENCE 509 AA; 58425 MW; 174FC39931AB5255 CRC64;
MTNTIVISCL HNMAAILYCG QIQKLVVANA HYQVSDIYLG CVDKIFSGIN AAFINLGKNE
YSGFIHISDT GPLKKKYYVN NITNILTIRQ KILVQIIKEP TLNKGPRLTA NITLSGRYIV
LMPFSQSICI SRKIYDEDER HYLKSLAILI KPATMGLLFR PSAVGVDEEI ILSELKNLKE
QWNFVQKSAI NSYSPVLLYK DEDIVKKVIR DFYNNNTNNI VIDSNLGLKQ LNYYIHTWHC
NNSSTVPKIK LYSNNQCILD AFGINQAISR ALIPKVDLIL GGYMFIETLE AFTIIDVNSG
SFNNSTSARE TVLKTNCSAA TEIAYQLQIR NITGVIIIDF IDMESQRDQL QLLEHFNKEL
SLDDAKPQIV QLSELGLVEL TRRRQGKSLY ELISSDSNYF YFFTQSERSQ SLKRFDDRQQ
KQQIFNKSWL SAEINTINKV FFQKSNLCRP ANFYLIRNLY IVKSSITYKQ NYLLTHRSKL
IYSKEYSKVL PSSYYLASLN KNSNQEFLS